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Q8K4D7 (PLCZ1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1

EC=3.1.4.11
Alternative name(s):
Phosphoinositide phospholipase C-zeta-1
Phospholipase C-zeta-1
Short name=PLC-zeta-1
Gene names
Name:Plcz1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length647 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. In vitro, hydrolyzes PtdIns(4,5)P2 in a Ca2+-dependent manner. Triggers intracellular Ca2+ oscillations in oocytes solely during M phase and is involved in inducing oocyte activation and initiating embryonic development up to the blastocyst stage. Is therefore a strong candidate for the egg-activating soluble sperm factor that is transferred from the sperm into the egg cytoplasm following gamete membrane fusion. May exert an inhibitory effect on phospholipase-C-coupled processes that depend on calcium ions and protein kinase C, including CFTR trafficking and function. Ref.1 Ref.2 Ref.5 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 UniProtKB Q86YW0

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. UniProtKB P10688

Cofactor

Calcium. Ref.8

Subunit structure

Interacts via its C2 domain with PtdIns3P and, to a lesser extent, PtdIns5P in vitro. Ref.8

Subcellular location

Nucleus. Cytoplasmperinuclear region. Note: Exhibits alternative cytoplasmic/nuclear localization during development. Translocates from the pronucleus into cytoplasm upon nuclear envelope breakdown for mitosis and localizes again to the pronuclei at interphase following meiosis and mitosis. Ref.2 Ref.5 Ref.6 Ref.7 Ref.13

Tissue specificity

Highly expressed in postpuberal testis, where expression is sperm cell-specific. Also expressed in brain of both sexes. Ref.1

Domain

The EF-hand and C2 domains are essential for triggering Ca2+ oscillating activity and the regulation of PLCZ1 enzyme activity. Ref.8 Ref.9 Ref.10 Ref.12

The X-Y linker region between PI-PLC X-box and Y-box domains may be a target for proteolysis and may play an important regulatory role during fertilization. Ref.8 Ref.9 Ref.10 Ref.12

Miscellaneous

Transgenic mice, where broad ectopic expression is forced, initially appear healthy and their oocytes undergo unperturbed meiotic maturation to metaphase II but subsequently exhibit autonomous intracellular free calcium oscillations, second polar body extrusion, pronucleus formation and parthenogenetic development. Transgenic males remained largely asymptomatic, whereas transgenic females develop abdominal swellings caused by benign ovarian teratomas.

Sequence similarities

Contains 1 C2 domain.

Contains 1 EF-hand domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 Ref.3 Ref.4 (identifier: Q8K4D7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.2 (identifier: Q8K4D7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6476471-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1
PRO_0000347246

Regions

Domain43 – 7836EF-hand
Domain163 – 307145PI-PLC X-box
Domain386 – 502117PI-PLC Y-box
Domain507 – 610104C2

Sites

Active site1781 By similarity UniProtKB P10688
Active site2231 By similarity UniProtKB P10688

Natural variations

Alternative sequence1 – 110110Missing in isoform 2. Ref.2
VSP_052863

Experimental info

Mutagenesis2101D → R: Defective in Ca(2+) oscillation activity and shows slower nuclear translocation. Ref.10
Mutagenesis2991K → E: Defective in Ca(2+) oscillation activity and loss of nuclear translocation. Ref.10
Mutagenesis3011K → E: Defective in Ca(2+) oscillation activity and loss of nuclear translocation. Ref.10
Mutagenesis3761R → E: Abolishes nuclear translocation. Ref.10
Mutagenesis3771K → E: Abolishes nuclear translocation. Prolongs Ca(2+) oscillations allowing them to occur during interphase. Ref.6 Ref.10
Mutagenesis3781R → E: Abolishes nuclear translocation. Ref.10
Mutagenesis3791K → E: Abolishes nuclear translocation. Ref.10
Mutagenesis3811K → E: Abolishes nuclear translocation. Ref.10
Sequence conflict581Q → H in AAI06768. Ref.4
Sequence conflict3601R → K in AAI06768. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: ABE24E5CCCC63CA2

FASTA64774,614
        10         20         30         40         50         60 
MESQLHELAE ARWFLSKVQD DFRGGKINVE ITHKLLEKLD FPCHFAHVKH IFKENDRQNQ 

        70         80         90        100        110        120 
GRITIEEFRA IYRCIVHREE ITEIFNTYTE NRKILSENSL IEFLTQEQYE MEIDHSDSVE 

       130        140        150        160        170        180 
IINKYEPIEE VKGERQMSIE GFARYMFSSE CLLFKENCKT VYQDMNHPLS DYFISSSHNT 

       190        200        210        220        230        240 
YLISDQILGP SDIWGYVSAL VKGCRCLEID CWDGSQNEPI VYHGYTFTSK LLFKTVVQAI 

       250        260        270        280        290        300 
NKYAFVTSDY PVVLSLENHC SPGQQEVMAS ILQSTFGDFL LSDMLEEFPD TLPSPEALKF 

       310        320        330        340        350        360 
KILVKNRKVG TLSETHERIG TDKSGQVLEW KEVIYEDGDE DSGMDPETWD VFLSRIKEER 

       370        380        390        400        410        420 
EADPSTLSGI AGVKKRKRKM KIAMALSDLV IYTKAEKFRN FQYSRVYQQF NETNSIGESR 

       430        440        450        460        470        480 
ARKLSKLRVH EFIFHTAAFI TRVYPKMMRA DSSNFNPQEF WNVGCQMVAL NFQTPGLPMD 

       490        500        510        520        530        540 
LQNGKFLDNG GSGYILKPDI LRDTTLGFNP NEPEYDDHPV TLTIRIISGI QLPVSSSSNT 

       550        560        570        580        590        600 
PDIVVIIEVY GVPNDHVKQQ TRVVKNNAFS PKWNETFTFL IQVPELALIR FVVETQQGLL 

       610        620        630        640 
SGNELLGQYT LPVLCMNKGY RRVPLFSKSG ANLEPSSLFI YVWYFRE 

« Hide

Isoform 2 [UniParc].

Checksum: 4B6832D35A65F75F
Show »

FASTA53761,307

References

« Hide 'large scale' references
[1]"PLC zeta: a sperm-specific trigger of Ca(2+) oscillations in eggs and embryo development."
Saunders C.M., Larman M.G., Parrington J., Cox L.J., Royse J., Blayney L.M., Swann K., Lai F.A.
Development 129:3533-3544(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Strain: C57BL/6J.
Tissue: Spermatid.
[2]"Recombinant phospholipase Czeta has high Ca2+ sensitivity and induces Ca2+ oscillations in mouse eggs."
Kouchi Z., Fukami K., Shikano T., Oda S., Nakamura Y., Takenawa T., Miyazaki S.
J. Biol. Chem. 279:10408-10412(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Testis.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Mammalian phospholipase Czeta induces oocyte activation from the sperm perinuclear matrix."
Fujimoto S., Yoshida N., Fukui T., Amanai M., Isobe T., Itagaki C., Izumi T., Perry A.C.F.
Dev. Biol. 274:370-383(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Cell cycle-dependent Ca2+ oscillations in mouse embryos are regulated by nuclear targeting of PLCzeta."
Larman M.G., Saunders C.M., Carroll J., Lai F.A., Swann K.
J. Cell Sci. 117:2513-2521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-377.
[7]"Nuclear translocation of phospholipase C-zeta, an egg-activating factor, during early embryonic development."
Sone Y., Ito M., Shirakawa H., Shikano T., Takeuchi H., Kinoshita K., Miyazaki S.
Biochem. Biophys. Res. Commun. 330:690-694(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta."
Kouchi Z., Shikano T., Nakamura Y., Shirakawa H., Fukami K., Miyazaki S.
J. Biol. Chem. 280:21015-21021(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR, INTERACTION WITH PTDINS(3)P AND PTDINS(5)P, DOMAIN.
[9]"Role of phospholipase C-zeta domains in Ca2+-dependent phosphatidylinositol 4,5-bisphosphate hydrolysis and cytoplasmic Ca2+ oscillations."
Nomikos M., Blayney L.M., Larman M.G., Campbell K., Rossbach A., Saunders C.M., Swann K., Lai F.A.
J. Biol. Chem. 280:31011-31018(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[10]"The role of X/Y linker region and N-terminal EF-hand domain in nuclear translocation and Ca2+ oscillation-inducing activities of phospholipase Czeta, a mammalian egg-activating factor."
Kuroda K., Ito M., Shikano T., Awaji T., Yoda A., Takeuchi H., Kinoshita K., Miyazaki S.
J. Biol. Chem. 281:27794-27805(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF ASP-210; LYS-299; LYS-301; ARG-376; LYS-377; ARG-378; LYS-379 AND LYS-381.
[11]"Broad, ectopic expression of the sperm protein PLCZ1 induces parthenogenesis and ovarian tumours in mice."
Yoshida N., Amanai M., Fukui T., Kajikawa E., Brahmajosyula M., Iwahori A., Nakano Y., Shoji S., Diebold J., Hessel H., Huss R., Perry A.C.
Development 134:3941-3952(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, OVEREXPRESSION.
[12]"Proteolytic processing of phospholipase Czeta and [Ca2+]i oscillations during mammalian fertilization."
Kurokawa M., Yoon S.Y., Alfandari D., Fukami K., Sato K., Fissore R.A.
Dev. Biol. 312:407-418(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN.
[13]"Difference in Ca2+ oscillation-inducing activity and nuclear translocation ability of PLCZ1, an egg-activating sperm factor candidate, between mouse, rat, human, and medaka fish."
Ito M., Shikano T., Oda S., Horiguchi T., Tanimoto S., Awaji T., Mitani H., Miyazaki S.
Biol. Reprod. 78:1081-1090(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF435950 mRNA. Translation: AAM95914.1.
AK006672 mRNA. No translation available.
BC106767 mRNA. Translation: AAI06768.1.
RefSeqNP_473407.2. NM_054066.4.
XP_006506966.1. XM_006506903.1.
UniGeneMm.50808.

3D structure databases

ProteinModelPortalQ8K4D7.
SMRQ8K4D7. Positions 25-645.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8K4D7.

Proteomic databases

PRIDEQ8K4D7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032356; ENSMUSP00000032356; ENSMUSG00000030230. [Q8K4D7-1]
GeneID114875.
KEGGmmu:114875.
UCSCuc009eny.1. mouse. [Q8K4D7-1]

Organism-specific databases

CTD89869.
MGIMGI:2150308. Plcz1.

Phylogenomic databases

eggNOGNOG149692.
GeneTreeENSGT00730000110266.
HOGENOMHOG000006871.
HOVERGENHBG053610.
InParanoidQ8K4D7.
KOK05861.
OMAHGRTWTS.
OrthoDBEOG7V49XT.
PhylomeDBQ8K4D7.
TreeFamTF313216.

Enzyme and pathway databases

BRENDA3.1.4.11. 3474.

Gene expression databases

BgeeQ8K4D7.
GenevestigatorQ8K4D7.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR001192. PI-PLC_fam.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR028395. PLC-zeta1.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF29. PTHR10336:SF29. 1 hit.
PfamPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio368899.
PROQ8K4D7.
SOURCESearch...

Entry information

Entry namePLCZ1_MOUSE
AccessionPrimary (citable) accession number: Q8K4D7
Secondary accession number(s): Q3KPE5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot